1EEH
UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
1EEH の概要
エントリーDOI | 10.2210/pdb1eeh/pdb |
関連するPDBエントリー | 1UAG 2UAG 3UAG 4UAG |
分子名称 | UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE (3 entities in total) |
機能のキーワード | ligase, peptidoglycan synthesis, murd, adp-forming enzyme |
由来する生物種 | Escherichia coli |
細胞内の位置 | Cytoplasm: P14900 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 47639.74 |
構造登録者 | Bertrand, J.A.,Fanchon, E.,Martin, L.,Chantalat, L.,Auger, G.,Blanot, D.,van Heijenoort, J.,Dideberg, O. (登録日: 2000-01-31, 公開日: 2001-01-17, 最終更新日: 2024-02-07) |
主引用文献 | Bertrand, J.A.,Fanchon, E.,Martin, L.,Chantalat, L.,Auger, G.,Blanot, D.,van Heijenoort, J.,Dideberg, O. "Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase. J.Mol.Biol., 301:1257-1266, 2000 Cited by PubMed Abstract: UDP-N-acetylmuramoyl-l-alanine:d-glutamate (MurD) ligase catalyses the addition of d-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-l-alanine (UMA). The crystal structures of Escherichia coli in the substrate-free form and MurD complexed with UMA have been determined at 2.4 A and 1.88 A resolution, respectively. The MurD structure comprises three domains each of a topology reminiscent of nucleotide-binding folds. In the two structures the C-terminal domain undergoes a large rigid-body rotation away from the N-terminal and central domains. These two "open" structures were compared with the four published "closed" structures of MurD. In addition the comparison reveals which regions are affected by the binding of UMA, ATP and d-Glu. Also we compare and discuss two structurally characterized enzymes which belong to the same ligase superfamily: MurD and folylpolyglutamate synthetase (FGS). The analysis allows the identification of key residues involved in the reaction mechanism of FGS. The determination of the two "open" conformation structures represents a new step towards the complete elucidation of the enzymatic mechanism of the MurD ligase. PubMed: 10966819DOI: 10.1006/jmbi.2000.3994 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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